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Conserved domains on  [gi|1915297359|dbj|BBW40153|]
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GTP 3',8-cyclase [Citrobacter portucalensis]

Protein Classification

GTP 3',8-cyclase MoaA( domain architecture ID 11478261)

GTP 3',8-cyclase MoaA catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z)

EC:  4.1.99.22
Gene Symbol:  moaA
PubMed:  8361352

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
9-340 0e+00

GTP 3',8-cyclase MoaA;


:

Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 531.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359   9 KVYMGSQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGgVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLR 88
Cdd:PRK00164    1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPF-LPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  89 RDFTDIIAAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFE 168
Cdd:PRK00164   80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 169 KVKVNTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVF 248
Cdd:PRK00164  160 PVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 249 CHPDYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNN 328
Cdd:PRK00164  240 RHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN 319
                         330
                  ....*....|..
gi 1915297359 329 TGITQNLSYIGG 340
Cdd:PRK00164  320 TGPTRHMSYIGG 331
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
9-340 0e+00

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 531.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359   9 KVYMGSQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGgVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLR 88
Cdd:PRK00164    1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPF-LPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  89 RDFTDIIAAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFE 168
Cdd:PRK00164   80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 169 KVKVNTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVF 248
Cdd:PRK00164  160 PVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 249 CHPDYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNN 328
Cdd:PRK00164  240 RHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN 319
                         330
                  ....*....|..
gi 1915297359 329 TGITQNLSYIGG 340
Cdd:PRK00164  320 TGPTRHMSYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
12-340 2.13e-160

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 451.44  E-value: 2.13e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  12 MGSQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGgVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDF 91
Cdd:COG2896     1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQF-LPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  92 TDIIAAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVK 171
Cdd:COG2896    80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 172 VNTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVFCHP 251
Cdd:COG2896   160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 252 DYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNN-TG 330
Cdd:COG2896   240 GGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDfPQ 319
                         330
                  ....*....|
gi 1915297359 331 ITQNLSYIGG 340
Cdd:COG2896   320 PKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
16-340 1.29e-139

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 398.91  E-value: 1.29e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  16 LTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDII 95
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  96 AAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAIT-GQDKFQQVMAGIDAAFDAGFEKVKVNT 174
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 175 VLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISG-QVLRDELLRRGWIHQIRQRSDG---PAQVFCH 250
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSAdEILERLEQAFGPLEPVPSPRGNgpaPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 251 PDYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTH----FLHQ 326
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHsflrFTSP 320
                         330
                  ....*....|....
gi 1915297359 327 NNTGITQNLSYIGG 340
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
197-323 1.77e-57

Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of Swiss:O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.


Pssm-ID: 428955 [Multi-domain]  Cd Length: 127  Bit Score: 182.03  E-value: 1.77e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 197 IQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVFCHPDYVGEIGLIMPYEKDFCATCNRLRV 276
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1915297359 277 SSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHF 323
Cdd:pfam06463  81 TADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
263-332 3.31e-27

Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding Twitch domain is found at the C-terminus of GTP 3',8-cyclase (EC 4.1.99.22), which is also called molybdenum cofactor biosynthesis protein A (MoaA) in bacteria and archaea, molybdenum cofactor biosynthesis protein 1 (MOCS1) in most eukaryotes, and molybdenum cofactor biosynthesis enzyme CNX2 in plants. GTP 3',8-cyclase is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the first step in molybdopterin biosynthesis, the cyclization of guanosine triphosphate to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate, which is then converted to molybdopterin in subsequent steps. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. GTP 3',8-cyclase contains an additional iron-sulfur cluster at the C-terminal Twitch domain that is involved in substrate binding. The Twitch domain may be related to another iron-sulfur cluster-binding domain found at the C-terminus of some radical SAM enzymes, the SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSMEs, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively.


Pssm-ID: 411052 [Multi-domain]  Cd Length: 70  Bit Score: 101.85  E-value: 3.31e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 263 YEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNNTGIT 332
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
26-173 1.77e-07

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 51.25  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359   26 YLRLSITDVCNFRCTYCLPDGYKPGGVTNNGFLTVDEIRRVTRAFASLG-TEKVRLTGGEPSL--RRDFTDIIAAVREND 102
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGEKEGlVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297359  103 AIRQ---IAVTTNGYRLARDAAAW-RDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVKVN 173
Cdd:smart00729  82 GLAKdveITIETRPDTLTEELLEAlKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTD 156
 
Name Accession Description Interval E-value
moaA PRK00164
GTP 3',8-cyclase MoaA;
9-340 0e+00

GTP 3',8-cyclase MoaA;


Pssm-ID: 234672 [Multi-domain]  Cd Length: 331  Bit Score: 531.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359   9 KVYMGSQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGgVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLR 88
Cdd:PRK00164    1 PVPMTSQLIDRFGRKFTYLRISVTDRCNFRCTYCMPEGYLPF-LPKEELLSLEEIERLVRAFVALGVRKVRLTGGEPLLR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  89 RDFTDIIAAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFE 168
Cdd:PRK00164   80 KDLEDIIAALAALPGIRDLALTTNGYLLARRAAALKDAGLDRVNVSLDSLDPERFKAITGRDRLDQVLAGIDAALAAGLT 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 169 KVKVNTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVF 248
Cdd:PRK00164  160 PVKVNAVLMKGVNDDEIPDLLEWAKDRGIQLRFIELMPTGEGNEWFRKHHLSGAEIRARLAERGWTLQPRARSGGPAQYF 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 249 CHPDYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNN 328
Cdd:PRK00164  240 RHPDYGGEIGLIAPVTHDFCASCNRLRLTADGKLHLCLFAEDGVDLRDLLRSGADDEELAAAIREALQNKPEGHGLHDGN 319
                         330
                  ....*....|..
gi 1915297359 329 TGITQNLSYIGG 340
Cdd:PRK00164  320 TGPTRHMSYIGG 331
MoaA COG2896
GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and ...
12-340 2.13e-160

GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) [Coenzyme transport and metabolism]; GTP 3',8-cyclase (molybdenum cofactor biosynthesis protein MoaA) is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 442141 [Multi-domain]  Cd Length: 329  Bit Score: 451.44  E-value: 2.13e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  12 MGSQLTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGgVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDF 91
Cdd:COG2896     1 MTSPLIDRFGRPIDYLRISVTDRCNFRCTYCMPEEGYQF-LPKEELLSFEEIERLVRAFVELGVRKIRLTGGEPLLRKDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  92 TDIIAAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVK 171
Cdd:COG2896    80 PELIARLAALPGIEDLALTTNGSLLARYAEALKAAGLDRVNVSLDSLDPERFRRITRRDDLDKVLAGIDAALAAGLTPVK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 172 VNTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVFCHP 251
Cdd:COG2896   160 INAVVMRGVNDDEILDLLEFAKERGIDLRFIELMPLGEGGGWRRDQVVSAAEILERLEARFPLEPLPARGGGPARYYRVP 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 252 DYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNN-TG 330
Cdd:COG2896   240 GGGGRIGFISPVSHPFCGSCNRLRLTADGKLRLCLFSEDEVDLRALLRSGASDEELAEAIREAIARKPEGHGFDEGDfPQ 319
                         330
                  ....*....|
gi 1915297359 331 ITQNLSYIGG 340
Cdd:COG2896   320 PKRSMSAIGG 329
moaA TIGR02666
molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes ...
16-340 1.29e-139

molybdenum cofactor biosynthesis protein A, bacterial; The model for this family describes molybdenum cofactor biosynthesis protein A, or MoaA, as found in bacteria. It does not include the family of probable functional equivalent proteins from the archaea. MoaA works together with MoaC to synthesize precursor Z from guanine. [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274250 [Multi-domain]  Cd Length: 334  Bit Score: 398.91  E-value: 1.29e-139
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  16 LTDAFARKFYYLRLSITDVCNFRCTYCLPDGYKPGGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDII 95
Cdd:TIGR02666   1 LIDRFGRRIDYLRISVTDRCNLRCVYCMPEGGGLDFLPKEELLTFEEIERLVRAFVGLGVRKVRLTGGEPLLRKDLVELV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  96 AAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAIT-GQDKFQQVMAGIDAAFDAGFEKVKVNT 174
Cdd:TIGR02666  81 ARLAALPGIEDIALTTNGLLLARHAKDLKEAGLKRVNVSLDSLDPERFAKITrRGGRLEQVLAGIDAALAAGLEPVKLNT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 175 VLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISG-QVLRDELLRRGWIHQIRQRSDG---PAQVFCH 250
Cdd:TIGR02666 161 VVMRGVNDDEIVDLAEFAKERGVTLRFIELMPLGEGNGWREKKFVSAdEILERLEQAFGPLEPVPSPRGNgpaPAYRWRL 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 251 PDYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTH----FLHQ 326
Cdd:TIGR02666 241 PGGKGRIGFISPVSDPFCGTCNRLRLTADGKLRLCLFADDGVDLRPLLRGGASDALLEAIIQAILQKKPEGHsflrFTSP 320
                         330
                  ....*....|....
gi 1915297359 327 NNTGITQNLSYIGG 340
Cdd:TIGR02666 321 ANKRRKRAMSQIGG 334
PLN02951 PLN02951
Molybderin biosynthesis protein CNX2
16-322 1.06e-80

Molybderin biosynthesis protein CNX2


Pssm-ID: 215513 [Multi-domain]  Cd Length: 373  Bit Score: 250.44  E-value: 1.06e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  16 LTDAFARKFYYLRLSITDVCNFRCTYCLPdgykPGGVT---NNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFT 92
Cdd:PLN02951   49 LVDSFGRRHNYLRISLTERCNLRCQYCMP----EEGVEltpKSHLLSQDEIVRLAGLFVAAGVDKIRLTGGEPTLRKDIE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  93 DIIAAVRENDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVKV 172
Cdd:PLN02951  125 DICLQLSSLKGLKTLAMTTNGITLSRKLPRLKEAGLTSLNISLDTLVPAKFEFLTRRKGHDRVLESIDTAIELGYNPVKV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 173 NTVLMRDVNHHQLDTFLAWIQPRPIQLRFIELMETgEGSSLFRKHHISGQVLRDELLRRgwIHQIRQRSDGPAQV---FC 249
Cdd:PLN02951  205 NCVVMRGFNDDEICDFVELTRDKPINVRFIEFMPF-DGNVWNVKKLVPYAEMMDRIEQR--FPSLKRLQDHPTDTaknFR 281
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297359 250 HPDYVGEIGLIMPYEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTH 322
Cdd:PLN02951  282 IDGHCGSVSFITSMTEHFCAGCNRLRLLADGNLKVCLFGPSEVSLRDALRSGADDDELREIIGAAVKRKKAAH 354
moaA_archaeal TIGR02668
probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an ...
16-312 4.77e-70

probable molybdenum cofactor biosynthesis protein A, archaeal; This model describes an archaeal family related, and predicted to be functionally equivalent, to molybdenum cofactor biosynthesis protein A (MoaA) of bacteria (see TIGR02666). [Biosynthesis of cofactors, prosthetic groups, and carriers, Molybdopterin]


Pssm-ID: 274251 [Multi-domain]  Cd Length: 302  Bit Score: 220.64  E-value: 4.77e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  16 LTDAFARKFYYLRLSITDVCNFRCTYCLPDGYkpgGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDII 95
Cdd:TIGR02668   1 LYDRFGRPVTSLRISVTDRCNLSCFYCHMEGE---DRSGGNELSPEEIERIVRVASEFGVRKVKITGGEPLLRKDLIEII 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  96 AAVReNDAIRQIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVKVNTV 175
Cdd:TIGR02668  78 RRIK-DYGIKDVSMTTNGILLEKLAKKLKEAGLDRVNVSLDTLDPEKYKKITGRGALDRVIEGIESAVDAGLTPVKLNMV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 176 LMRDVNHHQLDTFLAWIQPRPIQLRFIELMETGEGSSLFRKHHISGQVLRDEllrrgwihqIRQRSDGPAQVFCH--PDY 253
Cdd:TIGR02668 157 VLKGINDNEIPDMVEFAAEGGAILQLIELMPPGEGEKEFKKYHEDIDPIEEE---------LEKMADRVRTRRMHnrPKY 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1915297359 254 V----GEIGLIMPYEK-DFCATCNRLRVSSVGKLHLCLFGEGG-VSLRDLL---EDDAQQPALEERIS 312
Cdd:TIGR02668 228 FipggVEVEVVKPMDNpVFCAHCTRLRLTSDGKLKTCLLRDDNlVDILDALrngEDDELREAFREAVA 295
Mob_synth_C pfam06463
Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. ...
197-323 1.77e-57

Molybdenum Cofactor Synthesis C; This region contains two iron-sulphur (3Fe-4S) binding sites. Mutations in this region of Swiss:O14940 cause MOCOD (Molybdenum Co-Factor Deficiency) type A.


Pssm-ID: 428955 [Multi-domain]  Cd Length: 127  Bit Score: 182.03  E-value: 1.77e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 197 IQLRFIELMETGEGSSLFRKHHISGQVLRDELLRRGWIHQIRQRSDGPAQVFCHPDYVGEIGLIMPYEKDFCATCNRLRV 276
Cdd:pfam06463   1 IDLRFIELMPVGEGNGWRRKKFVSLDEILERIEARFPLLPARKRTGGPAKRYRIPGGGGRIGFIAPVSNPFCASCNRLRL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1915297359 277 SSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHF 323
Cdd:pfam06463  81 TADGKLKTCLFAEDGIDLRDALRSGDDDEELREAIREALARKPPRHS 127
SkfB COG0535
Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, ...
26-176 1.36e-28

Radical SAM superfamily maturase, SkfB/NifB/PqqE family [Cell cycle control, cell division, chromosome partitioning, Coenzyme transport and metabolism];


Pssm-ID: 440301 [Multi-domain]  Cd Length: 159  Bit Score: 108.45  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  26 YLRLSITDVCNFRCTYClpdgYKPGGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIr 105
Cdd:COG0535     1 RLQIELTNRCNLRCKHC----YADAGPKRPGELSTEEAKRILDELAELGVKVVGLTGGEPLLRPDLFELVEYAKELGIR- 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1915297359 106 qIAVTTNGYRLARDAAAW-RDAGLTALNVSVDSLDARQFHAITGQDK-FQQVMAGIDAAFDAGFeKVKVNTVL 176
Cdd:COG0535    76 -VNLSTNGTLLTEELAERlAEAGLDHVTISLDGVDPETHDKIRGVPGaFDKVLEAIKLLKEAGI-PVGINTVY 146
Twitch_MoaA cd21117
Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding ...
263-332 3.31e-27

Iron-sulfur cluster-binding Twitch domain of GTP 3',8-cyclase; The iron-sulfur cluster-binding Twitch domain is found at the C-terminus of GTP 3',8-cyclase (EC 4.1.99.22), which is also called molybdenum cofactor biosynthesis protein A (MoaA) in bacteria and archaea, molybdenum cofactor biosynthesis protein 1 (MOCS1) in most eukaryotes, and molybdenum cofactor biosynthesis enzyme CNX2 in plants. GTP 3',8-cyclase is a radical S-adenosylmethionine (SAM) enzyme that catalyzes the first step in molybdopterin biosynthesis, the cyclization of guanosine triphosphate to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate, which is then converted to molybdopterin in subsequent steps. Radical SAM enzymes are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster that is involved in the reductive cleavage of SAM and generates a 5'-deoxyadenosyl radical, which in turn abstracts a hydrogen from the appropriately positioned carbon atom of the substrate. GTP 3',8-cyclase contains an additional iron-sulfur cluster at the C-terminal Twitch domain that is involved in substrate binding. The Twitch domain may be related to another iron-sulfur cluster-binding domain found at the C-terminus of some radical SAM enzymes, the SPASM domain, named after the biochemically characterized members, AlbA, PqqE, anSMEs, and MftC, which are involved in Subtilosin A, Pyrroloquinoline quinone, Anaerobic Sulfatase, and Mycofactocin maturation, respectively.


Pssm-ID: 411052 [Multi-domain]  Cd Length: 70  Bit Score: 101.85  E-value: 3.31e-27
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 263 YEKDFCATCNRLRVSSVGKLHLCLFGEGGVSLRDLLEDDAQQPALEERISAALLEKKQTHFLHQNNTGIT 332
Cdd:cd21117     1 MSEHFCASCNRLRLTADGKLKPCLFGDEEVDLRDALRSGASDEELREAIRAAVQRKPERHSLERGDSGTR 70
Radical_SAM pfam04055
Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual ...
31-186 1.56e-25

Radical SAM superfamily; Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation.


Pssm-ID: 427681 [Multi-domain]  Cd Length: 159  Bit Score: 100.29  E-value: 1.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  31 ITDVCNFRCTYClpDGYKPGGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDIIAAV--RENDAIRQIA 108
Cdd:pfam04055   1 ITRGCNLRCTYC--AFPSIRARGKGRELSPEEILEEAKELKRLGVEVVILGGGEPLLLPDLVELLERLlkLELAEGIRIT 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1915297359 109 VTTNGYRLARDAAAW-RDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVKVNTVLMRDVNHHQLD 186
Cdd:pfam04055  79 LETNGTLLDEELLELlKEAGLDRVSIGLESGDDEVLKLINRGHTFEEVLEALELLREAGIPVVTDNIVGLPGETDEDLE 157
Radical_SAM cd01335
Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S ...
29-209 7.87e-12

Radical SAM superfamily. Enzymes of this family generate radicals by combining a 4Fe-4S cluster and S-adenosylmethionine (SAM) in close proximity. They are characterized by a conserved CxxxCxxC motif, which coordinates the conserved iron-sulfur cluster. Mechanistically, they share the transfer of a single electron from the iron-sulfur cluster to SAM, which leads to its reductive cleavage to methionine and a 5'-deoxyadenosyl radical, which, in turn, abstracts a hydrogen from the appropriately positioned carbon atom. Depending on the enzyme, SAM is consumed during this process or it is restored and reused. Radical SAM enzymes catalyze steps in metabolism, DNA repair, the biosynthesis of vitamins and coenzymes, and the biosynthesis of many antibiotics. Examples are biotin synthase (BioB), lipoyl synthase (LipA), pyruvate formate-lyase (PFL), coproporphyrinogen oxidase (HemN), lysine 2,3-aminomutase (LAM), anaerobic ribonucleotide reductase (ARR), and MoaA, an enzyme of the biosynthesis of molybdopterin.


Pssm-ID: 100105 [Multi-domain]  Cd Length: 204  Bit Score: 63.51  E-value: 7.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  29 LSITDVCNFRCTYCLPDGyKPGGVTNNGFLTVDEIRRVtRAFASLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAIRQIA 108
Cdd:cd01335     1 LELTRGCNLNCGFCSNPA-SKGRGPESPPEIEEILDIV-LEAKERGVEVVILTGGEPLLYPELAELLRRLKKELPGFEIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 109 VTTNG-YRLARDAAAWRDAGLTALNVSVDSLDARQFHAITG-QDKFQQVMAGIDAAFDAGFekvKVNTVLMRDVNHHQLD 186
Cdd:cd01335    79 IETNGtLLTEELLKELKELGLDGVGVSLDSGDEEVADKIRGsGESFKERLEALKELREAGL---GLSTTLLVGLGDEDEE 155
                         170       180       190
                  ....*....|....*....|....*....|
gi 1915297359 187 TFLAWIQ-------PRPIQLRFIELMETGE 209
Cdd:cd01335   156 DDLEELEllaefrsPDRVSLFRLLPEEGTP 185
AslB COG0641
Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, ...
29-285 2.72e-11

Sulfatase maturation enzyme AslB, radical SAM superfamily [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440406 [Multi-domain]  Cd Length: 349  Bit Score: 63.85  E-value: 2.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  29 LSITDVCNFRCTYClpdGYKPGGVTNNGFLTVDEIRRVTRAFA--SLGTEKVRLT--GGEPSLRRDF----TDIIAAVRE 100
Cdd:COG0641     5 LKPTSRCNLRCSYC---YYSEGDEGSRRRMSEETAEKAIDFLIesSGPGKELTITffGGEPLLNFDFikeiVEYARKYAK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 101 NDAIRQIAVTTNGYRLARDAAAWrdagLTALNVSVD-SLDARQ-FH-----AITGQDKFQQVMAGIDAAFDAGFEkVKVN 173
Cdd:COG0641    82 KGKKIRFSIQTNGTLLDDEWIDF----LKENGFSVGiSLDGPKeIHdrnrvTKNGKGSFDRVMRNIKLLKEHGVE-VNIR 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 174 TVLMRDvNHHQLDTFLAWIQPRPIQ-LRFIELMETGEGSSLFRKHHIsGQVLRdELLRRgWIhqirqRSDGPAQVFCHpd 252
Cdd:COG0641   157 CTVTRE-NLDDPEELYDFLKELGFRsIQFNPVVEEGEADYSLTPEDY-GEFLI-ELFDE-WL-----ERDGGKIFVRE-- 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1915297359 253 YVGEIGLIMPYEKDFC-ATCNR-LRVSSVGKLHLC 285
Cdd:COG0641   226 FDILLAGLLPPCSSPCvGAGGNyLVVDPDGDIYPC 260
SCM_rSAM_ScmF TIGR04251
SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in ...
24-289 1.18e-09

SynChlorMet cassette radical SAM/SPASM protein ScmF; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the more distant in sequence.


Pssm-ID: 211974 [Multi-domain]  Cd Length: 353  Bit Score: 58.70  E-value: 1.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  24 FYYLrlsiTDVCNFRCTYCLPDGYKPGGVTNNGFLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDIIAAVRENDA 103
Cdd:TIGR04251   7 YFYL----TEGCNLKCRHCWIDPKYQGEGEQHPSLDPSLFRSIIRQAIPLGLTSVKLTGGEPLLHPAIGEILECIGENNL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 104 irQIAVTTNGYrLARDAAAWRDAGLTALNVSV--DSLDARQFHAITG-QDKFQQVMAGIDAAFDAGFEKVKVNTVLMRDV 180
Cdd:TIGR04251  83 --QLSVETNGL-LCTPQTARDLASCETPFVSVslDGVDAATHDWMRGvKGAFDKAVRGIHNLVEAGIHPQIIMTVTRRNV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 181 NH-----HQLDTFLAwiqprpIQLRFIELMETGEGSSLFRkhhiSGQVLR-DELLRRG-WIHQIRQRSDGPAQVFCHPDY 253
Cdd:TIGR04251 160 GQmeqivRLAESLGA------ESVKFNHVQPTSRGSKMHE----NGETLSiGELVALGeWMERTLIPSTALRIDFGHPPA 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1915297359 254 VGEIGLIMPYEKDFCATCNRLRVSSV---GKLHLCLFGE 289
Cdd:TIGR04251 230 FRPLGRMFGEKPGGCGLCGIFGILGVlsdGSYALCGIGE 268
Elp3 smart00729
Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, ...
26-173 1.77e-07

Elongator protein 3, MiaB family, Radical SAM; This superfamily contains MoaA, NifB, PqqE, coproporphyrinogen III oxidase, biotin synthase and MiaB families, and includes a representative in the eukaryotic elongator subunit, Elp-3. Some members of the family are methyltransferases.


Pssm-ID: 214792 [Multi-domain]  Cd Length: 216  Bit Score: 51.25  E-value: 1.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359   26 YLRLSITDVCNFRCTYCLPDGYKPGGVTNNGFLTVDEIRRVTRAFASLG-TEKVRLTGGEPSL--RRDFTDIIAAVREND 102
Cdd:smart00729   2 LALYIITRGCPRRCTFCSFPSLRGKLRSRYLEALVREIELLAEKGEKEGlVGTVFIGGGTPTLlsPEQLEELLEAIREIL 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1915297359  103 AIRQ---IAVTTNGYRLARDAAAW-RDAGLTALNVSVDSLDARQFHAITGQDKFQQVMAGIDAAFDAGFEKVKVN 173
Cdd:smart00729  82 GLAKdveITIETRPDTLTEELLEAlKEAGVNRVSLGVQSGDDEVLKAINRGHTVEDVLEAVELLREAGPIKVSTD 156
PflA COG1180
Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, ...
35-201 2.55e-07

Pyruvate-formate lyase-activating enzyme [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440793 [Multi-domain]  Cd Length: 242  Bit Score: 50.95  E-value: 2.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  35 CNFRCTYCL-PDGYKPGGVTNNGFLTVDEIRRVTRAFASL--GTEKVRLTGGEPSLRRDFT-DIIAAVRENDaIRqIAVT 110
Cdd:COG1180    31 CNLRCPYCHnPEISQGRPDAAGRELSPEELVEEALKDRGFldSCGGVTFSGGEPTLQPEFLlDLAKLAKELG-LH-TALD 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 111 TNGYrLARDAAAWRDAGLTALNVSVDSLDARQFHAITGQDkFQQVMAGIDAAFDAGFEkVKVNTVLMRDVN--HHQLDTF 188
Cdd:COG1180   109 TNGY-IPEEALEELLPYLDAVNIDLKAFDDEFYRKLTGVS-LEPVLENLELLAESGVH-VEIRTLVIPGLNdsEEELEAI 185
                         170
                  ....*....|....*...
gi 1915297359 189 LAWIQP----RPIQL-RF 201
Cdd:COG1180   186 ARFIAElgdvIPVHLlPF 203
Tyw1 COG0731
Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal ...
34-204 2.89e-07

Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily [Translation, ribosomal structure and biogenesis]; Wyosine [tRNA(Phe)-imidazoG37] synthetase, radical SAM superfamily is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440495 [Multi-domain]  Cd Length: 248  Bit Score: 50.96  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  34 VCNFRCTYC-LPdgyKPGGVTNNG--FLTVDEIRR-VTRAFASLGTEKVRL-----TG-GEPSLRRDFTDIIAAVRENDA 103
Cdd:COG0731    33 TCNFDCVYCqRG---RTTDLTRERreFDDPEEILEeLIEFLRKLPEEAREPdhitfSGsGEPTLYPNLGELIEEIKKLRG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359 104 IRqIAVTTNGYRLARDAAAWRDAGLTALNVSVDSLDARQFHAIT---GQDKFQQVMAGIDAAFDAGFEKVKVNTVLMRDV 180
Cdd:COG0731   110 IK-TALLTNGSLLHRPEVREELLKADQVYPSLDAADEETFRKINrphPGLSWERIIEGLELFRKLYKGRTVIETMLVKGI 188
                         170       180
                  ....*....|....*....|....*.
gi 1915297359 181 N--HHQLDTFLAWIqpRPIQLRFIEL 204
Cdd:COG0731   189 NdsEEELEAYAELI--KRINPDFVEL 212
QueE COG0602
Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic ...
35-113 3.24e-06

Organic radical activating enzyme NrdG/QueE [Coenzyme transport and metabolism]; Organic radical activating enzyme NrdG/QueE is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440367 [Multi-domain]  Cd Length: 205  Bit Score: 47.05  E-value: 3.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  35 CNFRCTYC------LPDGYKpggvtnngFLTVDEIrrVTRAfASLGTEKVRLTGGEPSLRRDFTDIIAAVRENDaiRQIA 108
Cdd:COG0602    30 CNLRCSWCdtkyawDGEGGK--------RMSAEEI--LEEV-AALGARHVVITGGEPLLQDDLAELLEALKDAG--YEVA 96

                  ....*
gi 1915297359 109 VTTNG 113
Cdd:COG0602    97 LETNG 101
ThiH COG1060
2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme ...
31-109 1.55e-05

2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE [Coenzyme transport and metabolism]; 2-iminoacetate synthase ThiH/Menaquinone biosynthesis enzymes MqnC and MqnE is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440680 [Multi-domain]  Cd Length: 351  Bit Score: 46.28  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  31 ITDVCNFRCTYC-------LPDGYKpggvtnngfLTVDEIRRVTRAFASLGTEKVRLTGGE-PSLRRD-FTDIIAAVREn 101
Cdd:COG1060    57 LTNVCVNGCKFCafsrdngDIDRYT---------LSPEEILEEAEEAKALGATEILLVGGEhPDLPLEyYLDLLRAIKE- 126

                  ....*...
gi 1915297359 102 dAIRQIAV 109
Cdd:COG1060   127 -RFPNIHI 133
TM0948 COG5014
Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General ...
22-157 3.34e-05

Uncharacterized conserved protein TM0948, MoaA-related, radical SAM superfamily [General function prediction only];


Pssm-ID: 444038  Cd Length: 261  Bit Score: 44.59  E-value: 3.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  22 RKFYYLR-------LSITDV--CNFRCTYCLPDGYKPGGVTNNGFLTVDEI-RRVTRAFASLGTEKVRLTGGEPSLRRD- 90
Cdd:COG5014    28 RKYYRFRggrwyggIATADVvgCNLRCGFCWSWRFRDFPLTIGKFYSPEEVaERLIEIARERGYRQVRLSGGEPTIGFEh 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1915297359  91 FTDIIAAVRENDAIrqIAVTTNG----YRLARDAAAWRDAGLTaLNVSVDSLDARQFHAITGQDKF---QQVMA 157
Cdd:COG5014   108 LLKVLELFSERGLT--FILETNGiligYDRELARELASFRNIV-VRVSIKGCTPEEFSMLTGADPEffeLQLRA 178
COG2100 COG2100
Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function ...
31-152 8.00e-05

Uncharacterized Fe-S cluster-containing enzyme, radical SAM superfamily [General function prediction only];


Pssm-ID: 441703 [Multi-domain]  Cd Length: 344  Bit Score: 43.74  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  31 ITDVCNFRCTYCLPD-GykPGGVTNNGFLTVD------EIRRVTRaFASLGTEkVRLTG-GEPSLRRDFTDIIAAVREND 102
Cdd:COG2100    42 PTTGCNLNCIFCSVDaG--PHSRTRQAEYIVDpeylveWFEKVAR-FKGKGVE-AHIDGvGEPLLYPYIVELVKGLKEIK 117
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1915297359 103 AIRQIAVTTNGYRLARDAAAW-RDAGLTALNVSVDSLDARQFHAITGQDKF 152
Cdd:COG2100   118 GVKVVSMQTNGTLLSEKLIDElEEAGLDRINLSIDTLDPEKAKKLAGTKWY 168
SCM_rSAM_ScmE TIGR04250
SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in ...
29-161 2.40e-04

SynChlorMet cassette radical SAM/SPASM protein ScmE; A biosynthesis cassette found in Syntrophobacter fumaroxidans MPOB, Chlorobium limicola DSM 245, Methanocella paludicola SANAE, and delta proteobacterium NaphS2 contains two PqqE-like radical SAM/SPASM domain proteins, a PqqD homolog, and a conserved hypothetical protein. These components suggest modification of a ribosomally produced peptide precursor, but the precursor has not been identified. Of the two PqqE homologs of the cassette, this family is the closer in sequence.


Pssm-ID: 211973 [Multi-domain]  Cd Length: 358  Bit Score: 42.54  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1915297359  29 LSITDVCNFRCTYClpDGYKPGGVTNNGfLTVDEIRRVTRAFASLGTEKVRLTGGEPSLRRDFTDIIAAVRENDAirQIA 108
Cdd:TIGR04250   7 IDITGRCNLRCRYC--SHFSSAAETPTD-LETAEWLRFFRELNRCSVLRVVLSGGEPFMRSDFREIIDGIVKNRM--RFS 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1915297359 109 VTTNGYRLARDAAAWRDAG--LTALNVSVDSLDARQFHAITGQDKFQQVMAGIDA 161
Cdd:TIGR04250  82 ILSNGTLITDAIASFLAATrrCDYVQVSIDGSTPGTHDRLRGTGSFLQAVEGIEL 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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